In mammals, Disabled proteins are adaptor molecules involved in the endocytosis of lipoprotein receptors – so they are important for several intracellular signalling pathways and for the uptake of nutrients by cells. Now, Jonathan Pettitt and colleagues (p. 2741) have thoroughly investigated the roles of the only Disabled orthologue in Caenorhabditis elegans, DAB-1. Using a null mutant, the researchers show that DAB-1 is essential for two well-characterised examples of endocytosis in C. elegans: the uptake of yolk proteins by oocytes, and the uptake of solutes by coelomocytes (macrophage-like scavenger cells). Looking more closely at the coelomocytes, the researchers see that DAB-1 colocalises with clathrin light chain, which is consistent with the idea that DAB-1 acts as an adaptor protein in clathrin-mediated endocytosis. In the oocytes, the mislocalisation of RME-2 (for receptor mediated endocytosis 2) in dab-1 mutants indicates that DAB-1 helps to organise RME-2 into compartments that can endocytose yolk protein. The results indicate that Disabled's function in receptor-mediated endocytosis is conserved in vertebrates and invertebrates. Furthermore, the researchers found genetic interactions between dab-1 and genes encoding other adaptor proteins (AP1 and AP3), raising the possibility that Disabled-mediated endocytosis also influences lysosomal trafficking.